An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis.

@article{Ray2004AnID,
  title={An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis.},
  author={Soumya S. Ray and Richard J Nowak and Konstantin Strokovich and R. H. Brown and Thomas Walz and Peter T. Lansbury},
  journal={Biochemistry},
  year={2004},
  volume={43 17},
  pages={4899-905}
}
Familial amyotrophic lateral sclerosis (FALS) is linked to over 90 point mutations in superoxide dismutase-1 (SOD1), a dimeric metalloenzyme. The postmortem FALS brain is characterized by SOD1 inclusions in the motor neurons of regions in which neuronal loss is most significant. These findings, together with animal modeling studies, suggest that aggregation of mutant SOD1 produces a pathogenic species. We demonstrate here that a mutant form of SOD1 (A4V) that is linked to a particularly… CONTINUE READING
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